MCSB_STAA8
ID MCSB_STAA8 Reviewed; 335 AA.
AC Q2G0P6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Protein-arginine kinase {ECO:0000255|HAMAP-Rule:MF_00602};
DE EC=2.7.14.1 {ECO:0000255|HAMAP-Rule:MF_00602};
GN Name=mcsB {ECO:0000255|HAMAP-Rule:MF_00602};
GN OrderedLocusNames=SAOUHSC_00504;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP INDUCTION, AND INTERACTION WITH MCSA AND CTSR.
RC STRAIN=SH1000;
RX PubMed=22126623; DOI=10.1111/j.1574-6968.2011.02468.x;
RA Sitthisak S., Kitti T., Boonyonying K., Wozniak D., Mongkolsuk S.,
RA Jayaswal R.K.;
RT "McsA and the roles of metal-binding motif in Staphylococcus aureus.";
RL FEMS Microbiol. Lett. 327:126-133(2012).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=RN4220;
RX PubMed=22902728; DOI=10.1099/mic.0.060749-0;
RA Wozniak D.J., Tiwari K.B., Soufan R., Jayaswal R.K.;
RT "The mcsB gene of the clpC operon is required for stress tolerance and
RT virulence in Staphylococcus aureus.";
RL Microbiology 158:2568-2576(2012).
CC -!- FUNCTION: Catalyzes the specific phosphorylation of arginine residues
CC in proteins (By similarity). Is required for stress tolerance and
CC virulence in S.aureus. Acts as a modulator of the repressor activity of
CC CtsR upon heavy metal and oxidative stress caused by these metal ions
CC (PubMed:22902728). {ECO:0000255|HAMAP-Rule:MF_00602,
CC ECO:0000269|PubMed:22902728}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-
CC arginyl-[protein]; Xref=Rhea:RHEA:43384, Rhea:RHEA-COMP:10532,
CC Rhea:RHEA-COMP:10533, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83226, ChEBI:CHEBI:456216;
CC EC=2.7.14.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00602};
CC -!- SUBUNIT: Interacts with McsA and CtsR. {ECO:0000269|PubMed:22126623}.
CC -!- INDUCTION: Up-regulated by heavy metals such as Cu(2+) and Cd(2+), but
CC Zn(2+) and Co(2+) have no effect. Forms part of an operon with ctsR,
CC mcsA and clpC, which is repressed by CtsR.
CC {ECO:0000269|PubMed:22126623, ECO:0000269|PubMed:22902728}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to heavy metal stress,
CC temperature stress, osmotic pressure stress and oxidative stress.
CC Deletion of mcsB also results in sensitivity to variations in pH and
CC lowered expression of the clpC operon under adverse extracellular
CC conditions. Additionally, virulence traits such as hemolytic activity,
CC proteolysis, biofilm formation, and evasion from peritoneal fluid
CC killing are substantially reduced in cells lacking this gene.
CC Interestingly, mutant cells also show a significant reduction in
CC expression of virulence determinants hla and saeS.
CC {ECO:0000269|PubMed:22902728}.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00602}.
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DR EMBL; CP000253; ABD29653.1; -; Genomic_DNA.
DR RefSeq; WP_000149503.1; NZ_LS483365.1.
DR RefSeq; YP_499077.1; NC_007795.1.
DR AlphaFoldDB; Q2G0P6; -.
DR SMR; Q2G0P6; -.
DR STRING; 1280.SAXN108_0577; -.
DR EnsemblBacteria; ABD29653; ABD29653; SAOUHSC_00504.
DR GeneID; 3920416; -.
DR KEGG; sao:SAOUHSC_00504; -.
DR PATRIC; fig|93061.5.peg.451; -.
DR eggNOG; COG3869; Bacteria.
DR HOGENOM; CLU_066591_1_0_9; -.
DR OMA; IIMQERV; -.
DR PRO; PR:Q2G0P6; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1990170; P:stress response to cadmium ion; IDA:UniProtKB.
DR GO; GO:1990169; P:stress response to copper ion; IDA:UniProtKB.
DR CDD; cd07930; bacterial_phosphagen_kinase; 1.
DR HAMAP; MF_00602; Prot_Arg_kinase; 1.
DR InterPro; IPR023660; Arg_Kinase.
DR InterPro; IPR000749; ATP-guanido_PTrfase.
DR InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11547; PTHR11547; 1.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Stress response; Transferase.
FT CHAIN 1..335
FT /note="Protein-arginine kinase"
FT /id="PRO_1000025879"
FT DOMAIN 21..244
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 24..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 166..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
FT BINDING 197..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00602"
SQ SEQUENCE 335 AA; 38610 MW; FB1B26912A0A64BA CRC64;
MTHNIHDNIS QWMKSNEETP IVMSSRIRLA RNLENHVHPL MYATENDGFR VINEVQDALP
NFELMRLDQM DQQSKMKMVA KHLISPELIK QPAAAVLVND DESLSVMINE EDHIRIQAMG
TDTTLQALYN QASSIDDELD RSLDISYDEQ LGYLTTCPTN IGTGMRASVM LHLPGLSIMK
RMTRIAQTIN RFGYTIRGIY GEGSQVYGHT YQVSNQLTLG KSELEIIETL TEVVNQIIHE
EKQIRQKLDT YNQLETQDRV FRSLGILQNC RMITMEEASY RLSEVKLGID LNYIELQNFK
FNELMVAIQS PFLLDEEDDK SVKEKRADIL REHIK
